1LGL

Solution structure of HERG-specific scorpion toxin BeKm-1

Summary for 1LGL

• Entry DOI: 10.2210/pdb1lgl/pdb
• NMR Information: BMRB: 5184
• Descriptor: BeKm-1 toxin (1 entity in total)
• Functional Keywords: alpha-beta motif, cysteine-knot motif, toxin
• Biological source: Mesobuthus eupeus (lesser Asian scorpion)
• Cellular location: Secreted: Q9BKB7
• Total number of polymer chains: 1
• Total formula weight: 4103.73

Authors

Korolokova, Y.V.,Bocharov, E.V.,Angelo, K.,Maslennikov, I.V.,Grinenko, O.V.,Lipkin, A.V.,Nosireva, E.D.,Pluzhnikov, K.A.,Olesen, S.-P.,Arseniev, A.S.,Grishin, E.V. (deposition date: 2002-04-16, release date: 2002-11-20, Last modification date: 2024-11-06)

Primary citation

Korolkova, Y.V.,Bocharov, E.V.,Angelo, K.,Maslennikov, I.V.,Grinenko, O.V.,Lipkin, A.V.,Nosyreva, E.D.,Pluzhnikov, K.A.,Olesen, S.P.,Arseniev, A.S.,Grishin, E.V.
New binding site on common molecular scaffold provides HERG channel specificity of scorpion toxin BeKm-1.
J.Biol.Chem., 277:43104-43109, 2002

PubMed Abstract: The scorpion toxin BeKm-1 is unique among a variety of known short scorpion toxins affecting potassium channels in its selective action on ether-a-go-go-related gene (ERG)-type channels. BeKm-1 shares the common molecular scaffold with other short scorpion toxins. The toxin spatial structure resolved by NMR consists of a short alpha-helix and a triple-stranded antiparallel beta-sheet. By toxin mutagenesis study we identified the residues that are important for the binding of BeKm-1 to the human ERG K+ (HERG) channel. The most critical residues (Tyr-11, Lys-18, Arg-20, Lys-23) are located in the alpha-helix and following loop whereas the "traditional" functional site of other short scorpion toxins is formed by residues from the beta-sheet. Thus the unique location of the binding site of BeKm-1 provides its specificity toward the HERG channel.

PubMed: 12151390
DOI: 10.1074/jbc.M204083200

Experimental method

SOLUTION NMR